TRITON X-100 EXTRACTIONS OF CENTRAL NERVOUS-SYSTEM MYELIN INDICATE A POSSIBLE ROLE FOR THE MINOR MYELIN PROTEINS IN THE STABILITY OF LAMELLAE
TRITON X-100 EXTRACTIONS OF CENTRAL NERVOUS-SYSTEM MYELIN INDICATE A POSSIBLE ROLE FOR THE MINOR MYELIN PROTEINS IN THE STABILITY OF LAMELLAE
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DOI：
10.1007/bf00973301
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发表时间：
1988-06-01
影响因子：
4.4
通讯作者：
BRAUN, PE
中科院分区：
文献类型：
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作者：
PEREYRA, PM;HORVATH, E;BRAUN, PE
在先前建立的分离细胞骨架蛋白的条件下，用Triton X-100提取分离的中枢神经系统髓鞘膜。尽管去除了大部分主要的髓鞘碱性蛋白(18.5 kDa)和蛋白脂蛋白，但处理后的髓鞘仍保留了大部分其特有的板层结构，这两种蛋白加在一起通常占总髓鞘蛋白的60%。该提取物残留物的SDS-PAGE图谱显示，富含Mr为30至60千道尔顿的蛋白质(Wolfgram组)。主要的髓鞘蛋白由免疫印迹抗体鉴定，还有2‘’3‘-环核苷酸3’-磷酸二酯酶(CNP)、肌动蛋白、微管蛋白、髓鞘相关糖蛋白(MGP)和21.5 kDa的MBP。CNP、21.5 kDa MBP、MGP和微管蛋白对Triton提取的总体行为与其他膜-骨骼复合体的行为相似，支持这些和其他次要的髓鞘蛋白可能是跨髓鞘几层相互作用的异分子复合体的观点。
Isolated CNS myelin membranes were extracted with Triton X-100 under conditions previously established for the isolation of cytoskeletal proteins. Treated myelin retained much of its characteristic lamellar structure despite the removal of most of the major myelin basic protein (18.5 kDa) and the proteolipid protein, which together normally constitute 60% of the total myelin protein. The SDS-PAGE profile of this extract residue demonstrated an enrichment in proteins of Mr 30 to 60 kilodaltons (the Wolfgram group). The major myelin proteins were identified by antibodies on Western immunoblots, as were the 2''3''-cyclic nucleotide 3''-phosphodiesterase (CNP), actin, tubulin, myelin-associated glycoprotein (MGP) and the 21.5 kDa MBP. The overall behavior of CNP, the 21.5 kDa MBP, MGP and tubulin towards Triton extraction is reminiscent of the behavior of other membrane-skeletal complexes, supporting the idea that these and other minor myelin proteins might be part of heteromolecular complexes with interactions spanning several lamellae of the myelin sheath.